Abstract
The total proteins of Spanish Improved, TMVโ2 and DHโ3โ30 varieties were extracted and hydrolysed with two group specific enzymes alphaโchymotrypsin and trypsin and a less specific enzyme, pepsin. Compared to casein, the proteins were highly resistant to hydrolysis by the group specific enzymes. However, the variety TMVโ2 was more susceptible to proteolysis than the other two varieties. While the ratio and extend of hydrolysis for pepsin was same in all the varieties they were different for alphaโchymotrypsin. Nitrogen solubility profile of the meals in water, 1 M NaCl and 2% sodium hexametaphosphate solutions did not show any marked difference. Gel filtration, DEAEโCellulose chromatography, analytical ultracentrifugation and polyacrylamide gel electrophoretic patterns of the proteins did not indicate any major differences. However, the relative proportions of different fractions differed among the varieties. Gel filtration indicated that Spanish Improved variety contain higher amounts of conarachins (15%). Such quantitative differences of the various fractions may be responsible for the observed difference in the resistance to hydrolysis by the proteolytic enzymes.